UniProtKB - P11349 (NARH_ECOLI)
Protein
Respiratory nitrate reductase 1 beta chain
Gene
narH
Organism
Escherichia coli (strain K12)
Status
Functioni
The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The beta chain is an electron transfer unit containing four cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit.
Catalytic activityi
- EC:1.7.5.1
Cofactori
Protein has several cofactor binding sites:- [4Fe-4S] cluster2 PublicationsNote: Binds 3 [4Fe-4S] clusters per subunit.2 Publications
- [3Fe-4S] cluster2 PublicationsNote: Binds 1 [3Fe-4S] cluster per subunit.2 Publications
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 16 | Iron-sulfur 1 (4Fe-4S)2 Publications | 1 | |
Metal bindingi | 19 | Iron-sulfur 1 (4Fe-4S)2 Publications | 1 | |
Metal bindingi | 22 | Iron-sulfur 1 (4Fe-4S)2 Publications | 1 | |
Metal bindingi | 26 | Iron-sulfur 2 (4Fe-4S)2 Publications | 1 | |
Metal bindingi | 184 | Iron-sulfur 3 (4Fe-4S)2 Publications | 1 | |
Metal bindingi | 187 | Iron-sulfur 3 (4Fe-4S)2 Publications | 1 | |
Metal bindingi | 192 | Iron-sulfur 3 (4Fe-4S)2 Publications | 1 | |
Metal bindingi | 196 | Iron-sulfur 4 (3Fe-4S)2 Publications | 1 | |
Metal bindingi | 217 | Iron-sulfur 4 (3Fe-4S)2 Publications | 1 | |
Metal bindingi | 223 | Iron-sulfur 4 (3Fe-4S)2 Publications | 1 | |
Metal bindingi | 227 | Iron-sulfur 3 (4Fe-4S)2 Publications | 1 | |
Metal bindingi | 244 | Iron-sulfur 2 (4Fe-4S)2 Publications | 1 | |
Metal bindingi | 247 | Iron-sulfur 2 (4Fe-4S)2 Publications | 1 | |
Metal bindingi | 259 | Iron-sulfur 2 (4Fe-4S)2 Publications | 1 | |
Metal bindingi | 263 | Iron-sulfur 1 (4Fe-4S)2 Publications | 1 |
GO - Molecular functioni
- 3 iron, 4 sulfur cluster binding Source: EcoCyc
- 4 iron, 4 sulfur cluster binding Source: EcoCyc
- electron transfer activity Source: EcoCyc
- metal ion binding Source: UniProtKB-KW
- nitrate reductase activity Source: EcoCyc
GO - Biological processi
- anaerobic respiration Source: EcoCyc
- nitrate assimilation Source: UniProtKB-KW
- nitrate metabolic process Source: EcoCyc
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Electron transport, Nitrate assimilation, Transport |
Ligand | 3Fe-4S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:NARH-MONOMER MetaCyc:NARH-MONOMER |
BRENDAi | 1.7.5.1, 2026 |
Protein family/group databases
TCDBi | 5.A.3.1.1, the prokaryotic molybdopterin-containing oxidoreductase (pmo) family |
Names & Taxonomyi
Protein namesi | Recommended name: Respiratory nitrate reductase 1 beta chain (EC:1.7.5.1)Alternative name(s): Nitrate reductase A subunit beta Quinol-nitrate oxidoreductase subunit beta |
Gene namesi | Name:narH Ordered Locus Names:b1225, JW1216 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
GO - Cellular componenti
- intrinsic component of membrane Source: EcoCyc
- intrinsic component of the cytoplasmic side of the plasma membrane Source: EcoCyc
- membrane Source: UniProtKB
- NarGHI complex Source: EcoCyc
Keywords - Cellular componenti
Cell membrane, MembranePathology & Biotechi
Chemistry databases
DrugBanki | DB07349, (1S)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PENTANOYLOXY)METHYL]ETHYL OCTANOATE DB04464, N-Formylmethionine |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000096720 | 1 – 512 | Respiratory nitrate reductase 1 beta chainAdd BLAST | 512 |
Proteomic databases
jPOSTi | P11349 |
PaxDbi | P11349 |
PRIDEi | P11349 |
Expressioni
Inductioni
By nitrate.
Interactioni
Subunit structurei
Dimer of heterotrimers each composed of an alpha, a beta and a gamma chain. Alpha and beta are catalytic chains; gamma chains are involved in binding the enzyme complex to the cytoplasmic membrane.
1 PublicationBinary interactionsi
Hide detailsP11349
With | #Exp. | IntAct |
---|---|---|
fadH [P42593] | 3 | EBI-555067,EBI-561933 |
narG [P09152] | 13 | EBI-555067,EBI-547248 |
narW [P19317] | 3 | EBI-555067,EBI-555088 |
narY [P19318] | 3 | EBI-555067,EBI-555059 |
narZ [P19319] | 6 | EBI-555067,EBI-547262 |
Protein-protein interaction databases
BioGRIDi | 4262231, 28 interactors 850147, 6 interactors |
ComplexPortali | CPX-1974, Nitrate reductase A complex |
DIPi | DIP-10312N |
IntActi | P11349, 15 interactors |
STRINGi | 511145.b1225 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P11349 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P11349 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 7 – 35 | 4Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd BLAST | 29 | |
Domaini | 175 – 206 | 4Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd BLAST | 32 | |
Domaini | 208 – 237 | 4Fe-4S ferredoxin-type 3PROSITE-ProRule annotationAdd BLAST | 30 |
Keywords - Domaini
RepeatPhylogenomic databases
eggNOGi | COG1140, Bacteria |
HOGENOMi | CLU_043374_5_2_6 |
InParanoidi | P11349 |
PhylomeDBi | P11349 |
Family and domain databases
CDDi | cd10557, NarH_beta-like, 1 hit |
Gene3Di | 1.10.3650.10, 1 hit |
InterProi | View protein in InterPro IPR017896, 4Fe4S_Fe-S-bd IPR029263, Nitr_red_bet_C IPR038262, Nitr_red_bet_C_sf IPR006547, NO3_Rdtase_bsu |
Pfami | View protein in Pfam PF13247, Fer4_11, 1 hit PF14711, Nitr_red_bet_C, 1 hit |
TIGRFAMsi | TIGR01660, narH, 1 hit |
PROSITEi | View protein in PROSITE PS51379, 4FE4S_FER_2, 3 hits |
i Sequence
Sequence statusi: Complete.
P11349-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKIRSQVGMV LNLDKCIGCH TCSVTCKNVW TSREGVEYAW FNNVETKPGQ
60 70 80 90 100
GFPTDWENQE KYKGGWIRKI NGKLQPRMGN RAMLLGKIFA NPHLPGIDDY
110 120 130 140 150
YEPFDFDYQN LHTAPEGSKS QPIARPRSLI TGERMAKIEK GPNWEDDLGG
160 170 180 190 200
EFDKLAKDKN FDNIQKAMYS QFENTFMMYL PRLCEHCLNP ACVATCPSGA
210 220 230 240 250
IYKREEDGIV LIDQDKCRGW RMCITGCPYK KIYFNWKSGK SEKCIFCYPR
260 270 280 290 300
IEAGQPTVCS ETCVGRIRYL GVLLYDADAI ERAASTENEK DLYQRQLDVF
310 320 330 340 350
LDPNDPKVIE QAIKDGIPLS VIEAAQQSPV YKMAMEWKLA LPLHPEYRTL
360 370 380 390 400
PMVWYVPPLS PIQSAADAGE LGSNGILPDV ESLRIPVQYL ANLLTAGDTK
410 420 430 440 450
PVLRALKRML AMRHYKRAET VDGKVDTRAL EEVGLTEAQA QEMYRYLAIA
460 470 480 490 500
NYEDRFVVPS SHRELAREAF PEKNGCGFTF GDGCHGSDTK FNLFNSRRID
510
AIDVTSKTEP HP
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 398 – 417 | DTKPV…RHYKR → EYQTGTARTETYAGDASLQT in AAA24195 (PubMed:2832376).CuratedAdd BLAST | 20 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M20147 Genomic DNA Translation: AAA24195.1 U00096 Genomic DNA Translation: AAC74309.1 AP009048 Genomic DNA Translation: BAA36095.1 X16181 Genomic DNA Translation: CAA34304.1 |
PIRi | F64869, RDECNB |
RefSeqi | NP_415743.1, NC_000913.3 WP_000702650.1, NZ_STEB01000023.1 |
Genome annotation databases
EnsemblBacteriai | AAC74309; AAC74309; b1225 BAA36095; BAA36095; BAA36095 |
GeneIDi | 48106267 945780 |
KEGGi | ecj:JW1216 eco:b1225 |
PATRICi | fig|1411691.4.peg.1056 |
Similar proteinsi
Cross-referencesi
Web resourcesi
Worthington enzyme manual |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M20147 Genomic DNA Translation: AAA24195.1 U00096 Genomic DNA Translation: AAC74309.1 AP009048 Genomic DNA Translation: BAA36095.1 X16181 Genomic DNA Translation: CAA34304.1 |
PIRi | F64869, RDECNB |
RefSeqi | NP_415743.1, NC_000913.3 WP_000702650.1, NZ_STEB01000023.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1Q16 | X-ray | 1.90 | B | 1-512 | [»] | |
1R27 | X-ray | 2.00 | B/D | 1-512 | [»] | |
1SIW | X-ray | 2.20 | B | 1-512 | [»] | |
1Y4Z | X-ray | 2.00 | B | 1-512 | [»] | |
1Y5I | X-ray | 1.90 | B | 1-512 | [»] | |
1Y5L | X-ray | 2.50 | B | 1-512 | [»] | |
1Y5N | X-ray | 2.50 | B | 1-512 | [»] | |
3EGW | X-ray | 1.90 | B | 1-509 | [»] | |
3IR5 | X-ray | 2.30 | B | 1-512 | [»] | |
3IR6 | X-ray | 2.80 | B | 1-512 | [»] | |
3IR7 | X-ray | 2.50 | B | 1-512 | [»] | |
SMRi | P11349 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4262231, 28 interactors 850147, 6 interactors |
ComplexPortali | CPX-1974, Nitrate reductase A complex |
DIPi | DIP-10312N |
IntActi | P11349, 15 interactors |
STRINGi | 511145.b1225 |
Chemistry databases
DrugBanki | DB07349, (1S)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PENTANOYLOXY)METHYL]ETHYL OCTANOATE DB04464, N-Formylmethionine |
Protein family/group databases
TCDBi | 5.A.3.1.1, the prokaryotic molybdopterin-containing oxidoreductase (pmo) family |
Proteomic databases
jPOSTi | P11349 |
PaxDbi | P11349 |
PRIDEi | P11349 |
Genome annotation databases
EnsemblBacteriai | AAC74309; AAC74309; b1225 BAA36095; BAA36095; BAA36095 |
GeneIDi | 48106267 945780 |
KEGGi | ecj:JW1216 eco:b1225 |
PATRICi | fig|1411691.4.peg.1056 |
Organism-specific databases
EchoBASEi | EB0633 |
Phylogenomic databases
eggNOGi | COG1140, Bacteria |
HOGENOMi | CLU_043374_5_2_6 |
InParanoidi | P11349 |
PhylomeDBi | P11349 |
Enzyme and pathway databases
BioCyci | EcoCyc:NARH-MONOMER MetaCyc:NARH-MONOMER |
BRENDAi | 1.7.5.1, 2026 |
Miscellaneous databases
EvolutionaryTracei | P11349 |
PROi | PR:P11349 |
Family and domain databases
CDDi | cd10557, NarH_beta-like, 1 hit |
Gene3Di | 1.10.3650.10, 1 hit |
InterProi | View protein in InterPro IPR017896, 4Fe4S_Fe-S-bd IPR029263, Nitr_red_bet_C IPR038262, Nitr_red_bet_C_sf IPR006547, NO3_Rdtase_bsu |
Pfami | View protein in Pfam PF13247, Fer4_11, 1 hit PF14711, Nitr_red_bet_C, 1 hit |
TIGRFAMsi | TIGR01660, narH, 1 hit |
PROSITEi | View protein in PROSITE PS51379, 4FE4S_FER_2, 3 hits |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | NARH_ECOLI | |
Accessioni | P11349Primary (citable) accession number: P11349 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1989 |
Last sequence update: | February 1, 1996 | |
Last modified: | December 2, 2020 | |
This is version 193 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references